|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
440-637 |
4.28e-88 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 273.41 E-value: 4.28e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 440 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAALRVSEGRARGLQEAARARELELEACSQELQRYRQ 519
Cdd:pfam06818 1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 520 EAEQLREKARHLDAEAAGLREPPVPPATTDPFLLAESDEAKVQRAAAGTGGSLRAQVERLRQELQREQRRGDEQRNSFEG 599
Cdd:pfam06818 81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 261399904 600 ERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQ 637
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-650 |
1.81e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 333 KLRDREAELQQLRDSVDESEAAVcqafgARQRRwpgEREDCASHAQQATQRVQRAQQllqlqvfqlqqEKRQLQDDFAQL 412
Cdd:COG1196 233 KLRELEAELEELEAELEELEAEL-----EELEA---ELAELEAELEELRLELEELEL-----------ELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 413 LQEREQLERRCATFEREQQELGPRLEETKWevcqksgEISLLKQQLKESQAELVQKGSELVALRVALREARAALRVSEGR 492
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 493 ARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREppvppattdpfLLAESDEAKVQRAAAgtggsl 572
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-----------RLERLEEELEELEEA------ 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261399904 573 RAQVERLRQELQREQRrgdEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQQLSLELEARELAD 650
Cdd:COG1196 430 LAELEEEEEEEEEALE---EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
329-609 |
8.68e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 329 VLEGKLRDREAELQQLRDSVDESEAAVcQAFGARQRRwpgeredcashAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDD 408
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELEL-EEAQAEEYE-----------LLAELARLEQDIARLEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 409 FAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAALRV 488
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 489 SEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREppvppattdpflLAESDEAKVQRAAAGT 568
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE------------EEEALLELLAELLEEA 472
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 261399904 569 GGSLRAQVERLRQELQREQRR--GDEQRNSFEGERLAWQAEKE 609
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLllLLEAEADYEGFLEGVKAALL 515
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-655 |
9.78e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 9.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 480
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 481 EARAALRVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREppvppaTTDPFLLAESDEAK 560
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA------ELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 561 VQRAAAGTGGSLRAQVERLRQELQREQRRgdeqRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQQLS 640
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250
....*....|....*
gi 261399904 641 LELEARELADLGLSE 655
Cdd:COG1196 463 ELLAELLEEAALLEA 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-652 |
1.75e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 330 LEGKLRDREAELQQLRDSVDESEAAVcqafgaRQRRWPGEREDCASHAQQAtqrvqraqqllqlqvfqlqqEKRQLQDDF 409
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEEL------EQLRKELEELSRQISALRK--------------------DLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 410 AQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQkgselvaLRVALREARAALRVS 489
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-------LREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 490 EGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREPPVPPATTDPFLLAESDEAKVQRAAAGTG 569
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 570 -GSLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQQLSLELEAR-- 646
Cdd:TIGR02168 896 lEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlk 975
|
330
....*....|
gi 261399904 647 ----ELADLG 652
Cdd:TIGR02168 976 rlenKIKELG 985
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
401-647 |
2.69e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 480
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 481 EARAAL-RVSEGRARGLQEAARAREL-------------ELEACSQELQRYRQEAEQLREKARHLDAEAAGLReppvppa 546
Cdd:TIGR02168 313 NLERQLeELEAQLEELESKLDELAEElaeleekleelkeELESLEAELEELEAELEELESRLEELEEQLETLR------- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 547 ttdpfllAESDEAKVQRAA-AGTGGSLRAQVERLRQELQR-EQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQ 624
Cdd:TIGR02168 386 -------SKVAQLELQIASlNNEIERLEARLERLEDRRERlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
250 260
....*....|....*....|...
gi 261399904 625 MYRRNRQLEQELQQLSLELEARE 647
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAE 481
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
401-645 |
4.44e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDFAQLLQEREQLERRCATFEREQQELGpRLEETKWE---VCQKSGEISLLKQQLkesqAELVQKGSELVALRV 477
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDeidVASAEREIAELEAEL----ERLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 478 ALREARAALRVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAglreppvppattDPFLLAESD 557
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL------------EERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 558 EAKVQRAAAgtggSLRAQVERLRQELQREQRRGDEQRNSF----EGERLAWQAEKEQVIRYQKQLQ-------HNYVQMY 626
Cdd:COG4913 761 DAVERELRE----NLEERIDALRARLNRAEEELERAMRAFnrewPAETADLDADLESLPEYLALLDrleedglPEYEERF 836
|
250 260
....*....|....*....|.
gi 261399904 627 RR--NRQLEQELQQLSLELEA 645
Cdd:COG4913 837 KEllNENSIEFVADLLSKLRR 857
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
456-645 |
4.63e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 456 QQLKESQAELVQKGSELVALR--VALREARAALRVSEGRARGLQEAARA--RELELEACSQELQRYRQEAEQLREKARHL 531
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 532 DAEAAGLREppvppattdpfllaESDEAKVQRAAAGTG--GSLRAQVERLRQELQREQRRGDEQRN-------------- 595
Cdd:COG4913 315 EARLDALRE--------------ELDELEAQIRGNGGDrlEQLEREIERLERELEERERRRARLEAllaalglplpasae 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 261399904 596 SFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQQLSLELEA 645
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
329-610 |
8.21e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 329 VLEGKLRDREAELQQLRDSVDESEAAVCQafgaRQRRWPGEREDCASHAQ---QATQRVQRaqqllqlqvfQLQQEKRQL 405
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEK----LTEEISELEKRLEEIEQlleELNKKIKD----------LGEEEQLRV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 406 QDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAA 485
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 486 LRVSEGRARGLQEAARARELELEACSQEL-------QRYRQEAEQLREKARHLDAEAAGLRE--PPVPPATTDPFLLAES 556
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREInelkrelDRLQEELQRLSEELADLNAAIAGIEAkiNELEEEKEDKALEIKK 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 261399904 557 DEAKVQRAAAGTgGSLRAQVERLRQELQR-EQRRGDEQRNSFEGERLAWQAEKEQ 610
Cdd:TIGR02169 453 QEWKLEQLAADL-SKYEQELYDLKEEYDRvEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
323-640 |
1.08e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 323 EALLHCVLEGKLRDREAELQQLRDSVDESEaavcqafgarqrrwpGEREDCASHAQQATQRVQRAQQllqlqvfqlqqEK 402
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAE---------------EELEELTAELQELEEKLEELRL-----------EV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 403 RQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSEL-------VAL 475
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeelESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 476 RVALREARAALRVSEGRARGLQEAARAR-------ELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREppvppatt 548
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLrskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK-------- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 549 dpfllaESDEAKVQrAAAGTGGSLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQVIRYQ------KQLQHNY 622
Cdd:TIGR02168 429 ------KLEEAELK-ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENL 501
|
330
....*....|....*...
gi 261399904 623 VQMYRRNRQLEQELQQLS 640
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLS 519
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-655 |
4.00e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 414 QEREQLERRCATFEREQQELGPRLEETKWEVCQKsgEISLLKQQLKESQAELVQKGSELVALRVALREARAALRVSEGRa 493
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEA--ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 494 rglqeaararelELEACSQELQRYRQEAEQLREKARHLDAEAAGLREPPvpPATTDPFLlaesdeakvqraaagtggSLR 573
Cdd:COG4913 339 ------------RLEQLEREIERLERELEERERRRARLEALLAALGLPL--PASAEEFA------------------ALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 574 AQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQhnyvqmyRRNRQLEQELQQLSLELEarelADLGL 653
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE-------RRKSNIPARLLALRDALA----EALGL 455
|
..
gi 261399904 654 SE 655
Cdd:COG4913 456 DE 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
401-647 |
7.07e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 480
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 481 EARAALRvseGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREppvppattdpfLLAESDEAK 560
Cdd:COG4942 101 AQKEELA---ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA-----------DLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 561 VQRAAAgtggslRAQVERLRQELQREQRRGDEQRNsfEGERLAWQAEKEQvIRYQKQLQhnyvQMYRRNRQLEQELQQLS 640
Cdd:COG4942 167 AELEAE------RAELEALLAELEEERAALEALKA--ERQKLLARLEKEL-AELAAELA----ELQQEAEELEALIARLE 233
|
....*..
gi 261399904 641 LELEARE 647
Cdd:COG4942 234 AEAAAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-655 |
3.35e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 414 QEREQLERRCATFEREQQELGPRLEEtkwevcqksgeislLKQQLKESQAELVQKGSELVALRVALREARAALRVSEGRA 493
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAE--------------LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 494 RGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREPpvppattdpfLLAESDEAKVQRAAAGtggSLR 573
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ----------IEQLKEELKALREALD---ELR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 574 AQVERLRQE-------LQREQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQQLSLELEAR 646
Cdd:TIGR02168 810 AELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
....*....
gi 261399904 647 ELADLGLSE 655
Cdd:TIGR02168 890 ALLRSELEE 898
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
401-651 |
4.45e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDFAQLLQE-REQLErrcatfEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVAL 479
Cdd:TIGR02168 203 KSLERQAEKAERYKElKAELR------ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 480 REARAALRVSEGRARGLQEAARARELELEACSQELQRYRQEAE----QLREKARHLDAEAAGLREppvppattdpfLLAE 555
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEeleaQLEELESKLDELAEELAE-----------LEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 556 SDEAKVQRAaagtggSLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQE 635
Cdd:TIGR02168 346 LEELKEELE------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
250
....*....|....*.
gi 261399904 636 LQQLSLELEARELADL 651
Cdd:TIGR02168 420 QQEIEELLKKLEEAEL 435
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
333-648 |
7.92e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 333 KLRDREAELQQLRDSVDESEAAVCQAFGARQrrwpgEREDCASHAQQATQRVQRAqqllqlqvfqlqqekrQLQDDFAQL 412
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEE-----ELEELEAELEELREELEKL----------------EKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 413 LQEREQLERRCATFEREQQELGPRLEETKwevcQKSGEISLLKQQLKESQAELVQkgselvALRVALREARAALRVSEGR 492
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEE------LLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 493 ARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAgLREPPVPP----------ATTDPFLLAESDEAKVQ 562
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER-LKEARLLLliaaallallGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 563 RAAAGTGGSLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQV----------IRYQKQLQHNYVQMYRRNRQL 632
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspeeLLELLDRIEELQELLREAEEL 359
|
330
....*....|....*.
gi 261399904 633 EQELQQLSLELEAREL 648
Cdd:COG4717 360 EEELQLEELEQEIAAL 375
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
370-539 |
2.02e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 370 REDCASHAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKwEVCQKSG 449
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE-AQIRGNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 450 --EISLLKQQLKESQAELVQKGSELVALRVALREARAALRVSEGRARGLQEAARAR----ELELEACSQELQRYRQEAEQ 523
Cdd:COG4913 337 gdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRD 416
|
170
....*....|....*.
gi 261399904 524 LREKARHLDAEAAGLR 539
Cdd:COG4913 417 LRRELRELEAEIASLE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
333-546 |
4.14e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 333 KLRDREAELQQLRDSVDE-----SEAAVCQAFGARQRRWpgeredcasHAQQATQRVQRAQQLLQLQVFQLQQEKRQLQD 407
Cdd:COG4913 246 DAREQIELLEPIRELAERyaaarERLAELEYLRAALRLW---------FAQRRLELLEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 408 DFAQLLQEREQLERRCATFEREQ-QELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRvalREARAAL 486
Cdd:COG4913 317 RLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR---AEAAALL 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 487 RVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLR----------EKARHLDAEAAGLREPPVPPA 546
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksniparlLALRDALAEALGLDEAELPFV 463
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
303-664 |
5.50e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 303 GSSSGGDRSPPPPPPPPPSDEALLHcvlegKLRDREAELQQLRDSVDEseaavcqafgarqrrwpgEREDCASHAQQATQ 382
Cdd:TIGR02169 653 GAMTGGSRAPRGGILFSRSEPAELQ-----RLRERLEGLKRELSSLQS------------------ELRRIENRLDELSQ 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 383 RVQRAQQLLQLQVFqlqqEKRQLQDDFAQLLQEREQLERRCATFEREQQElgprleetkwevcqksgeislLKQQLKESQ 462
Cdd:TIGR02169 710 ELSDASRKIGEIEK----EIEQLEQEEEKLKERLEELEEDLSSLEQEIEN---------------------VKSELKELE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 463 AELVQKGSELVALRVAL-----REARAALRVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHldaeaag 537
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE------- 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 538 lreppvppattdpfLLAESDEAKVQRAAAG-TGGSLRAQVERLRQELQREQ---RRGDEQRNSFEGERLAWQAEKEQVIR 613
Cdd:TIGR02169 838 --------------LQEQRIDLKEQIKSIEkEIENLNGKKEELEEELEELEaalRDLESRLGDLKKERDELEAQLRELER 903
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 261399904 614 YQKQLQHNYVQMYRRNRQLEQELQQLSLELEARELADLGLSEPAPCICLEE 664
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE 954
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
336-655 |
1.34e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 336 DREAELQQLRDSVDESE---AAVCQAFGARQRRwpgeredcASHAQQATQRVQRAQQLLQLQVFQLQQEK---RQLQDDF 409
Cdd:PRK04863 380 ENEARAEAAEEEVDELKsqlADYQQALDVQQTR--------AIQYQQAVQALERAKQLCGLPDLTADNAEdwlEEFQAKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 410 AQLLQEREQLERRCATFE--REQQELGPRLeetkweVCQKSGEISllKQQLKESQAELVQKGSELVALRVALREARAALR 487
Cdd:PRK04863 452 QEATEELLSLEQKLSVAQaaHSQFEQAYQL------VRKIAGEVS--RSEAWDVARELLRRLREQRHLAEQLQQLRMRLS 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 488 VSEGRargLQEAARARELELEACSQ---------ELQRYRQEAEQLREkarHLDAEAAGLREppvppattdpfllaesde 558
Cdd:PRK04863 524 ELEQR---LRQQQRAERLLAEFCKRlgknlddedELEQLQEELEARLE---SLSESVSEARE------------------ 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 559 akvQRAAagtggsLRAQVERLRQELQREQRRGDEQRNSFEG-ERL-----AWQAEKEQVIRYQKQLQHNYVQMYRRNRQL 632
Cdd:PRK04863 580 ---RRMA------LRQQLEQLQARIQRLAARAPAWLAAQDAlARLreqsgEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
330 340
....*....|....*....|...
gi 261399904 633 EQELQQlsLELEARELADLGLSE 655
Cdd:PRK04863 651 AARKQA--LDEEIERLSQPGGSE 671
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
401-644 |
6.78e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDFAQLLQE-REQLERRCATFEREQQELGPRLEETK--WEV-CQKSGEISLLKQQLKESQAElVQKgseLVALR 476
Cdd:pfam15921 360 EARTERDQFSQESGNlDDQLQKLLADLHKREKELSLEKEQNKrlWDRdTGNSITIDHLRRELDDRNME-VQR---LEALL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 477 VALREAraalrvSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLR--EPPVPPATTDpflLA 554
Cdd:pfam15921 436 KAMKSE------CQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEssERTVSDLTAS---LQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 555 ESDEAKVQRAAAGTggSLRAQVERLRQELQREQRRGDEQRN-SFEGERLAWQ-AEKEQVIRYQKQLQHNYVQ-------- 624
Cdd:pfam15921 507 EKERAIEATNAEIT--KLRSRVDLKLQELQHLKNEGDHLRNvQTECEALKLQmAEKDKVIEILRQQIENMTQlvgqhgrt 584
|
250 260
....*....|....*....|...
gi 261399904 625 ---MYRRNRQLEQELQQLSLELE 644
Cdd:pfam15921 585 agaMQVEKAQLEKEINDRRLELQ 607
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
330-487 |
8.36e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 330 LEGKLRDREAELQQLRDSVDESEAAVCQAFGARQ--RRwpgEREDCASHAQQATQRVQRAqqllqlqvfqlqqEKRQLQ- 406
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEdlEK---EIKRLELEIEEVEARIKKY-------------EEQLGNv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 407 ---DDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREAR 483
Cdd:COG1579 86 rnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....
gi 261399904 484 AALR 487
Cdd:COG1579 166 EELA 169
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
401-588 |
8.63e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 480
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 481 EA-------RAALRVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREPPVPPATTDPFLL 553
Cdd:PRK02224 339 AHneeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418
|
170 180 190
....*....|....*....|....*....|....*
gi 261399904 554 AESDEAKVQRAaagtggSLRAQVERLRQELQREQR 588
Cdd:PRK02224 419 EERDELREREA------ELEATLRTARERVEEAEA 447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
374-619 |
8.78e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 374 ASHAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISL 453
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 454 LKQQLKESQAELVQkgsELVALRVALREARAALRVSegrARGLQEAARARELE---LEACSQELQRYRQEAEQLREKARH 530
Cdd:COG4942 95 LRAELEAQKEELAE---LLRALYRLGRQPPLALLLS---PEDFLDAVRRLQYLkylAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 531 LDAEAAGLREppvppattdpfllaesdeakvqraaagtggsLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQ 610
Cdd:COG4942 169 LEAERAELEA-------------------------------LLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
....*....
gi 261399904 611 VIRYQKQLQ 619
Cdd:COG4942 218 LQQEAEELE 226
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
415-651 |
9.24e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 415 EREQLER---RCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELvqkgSELVALRVALREARAALRVSEG 491
Cdd:PRK03918 177 RIERLEKfikRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 492 RARGLQEAARARE---LELEACSQELQRYRQEAEQLREKARhldaEAAGLREppvppattdpfLLAESDEAKVQraaagt 568
Cdd:PRK03918 253 SKRKLEEKIRELEeriEELKKEIEELEEKVKELKELKEKAE----EYIKLSE-----------FYEEYLDELRE------ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 569 ggsLRAQVERLRQELQREQRRGDEqRNSFEgERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQQLSLELEAREL 648
Cdd:PRK03918 312 ---IEKRLSRLEEEINGIEERIKE-LEEKE-ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
|
...
gi 261399904 649 ADL 651
Cdd:PRK03918 387 EKL 389
|
|
| CC149 |
pfam09789 |
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ... |
506-644 |
1.23e-05 |
|
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as being coiled-coil domain-containing protein 149, however they currently have no known function.
Pssm-ID: 462902 [Multi-domain] Cd Length: 314 Bit Score: 47.71 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 506 ELEACSQELQRYRQEAEQLREKARHLDAEAAGLRE--PPVPPATTDPF----LLAESDEAKVQraaagtggsLRAQVERL 579
Cdd:pfam09789 17 ELEKCRQERDQYKLMAEQLQERYQGLKKQLRELKAgnNDFKPDDREQVnliqLLRDSREQNKC---------LRLEVEEL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261399904 580 RQELQ---------REQ----RRGDEQRNSFeGERLAWQAEKEQVIryqKQLQhnyvQMYRRNRQLEQELQQLSLELE 644
Cdd:pfam09789 88 RQKLNeaqgdikllREQiarqRLGGPDEGSI-STRHFPLHEREELV---KQLE----KLRKKCQQLERDLQSVLDEKE 157
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
333-550 |
1.41e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 333 KLRDREAELQQLRDSVDESEAAVCQAFGARQRrwpgeredcashAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDDFAQL 412
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKA------------LLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 413 LQEREQLERRcatFEREQQELGPRLEETkwevcQKSGEISLLK-----------------------------QQLKESQA 463
Cdd:COG4942 89 EKEIAELRAE---LEAQKEELAELLRAL-----YRLGRQPPLAlllspedfldavrrlqylkylaparreqaEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 464 ELVQKGSELVALRVALREARAALrvsEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREPPV 543
Cdd:COG4942 161 ELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*..
gi 261399904 544 PPATTDP 550
Cdd:COG4942 238 AAAERTP 244
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
401-536 |
1.56e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 480
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 261399904 481 EARAALRVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAA 536
Cdd:COG4372 126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
330-650 |
2.75e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 330 LEGKLRDREAELQQLRDSVDESEAAVcqafgaRQRRwpGEREDCASHAQQATQRVQRAQQLLQLQV---FQLQQEKRQLQ 406
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEEL------EQAR--SELEQLEEELEELNEQLQAAQAELAQAQeelESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 407 DDFAQLLQEREQLERRCATFEREQQELgprleetKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAAL 486
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAEL-------QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 487 RVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREPPVPPATTDPFLLAESDEAKVQRAAA 566
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 567 GTGGSLRAQVERLRQELQREQRR-GDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQQLSLELEA 645
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEaALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
....*
gi 261399904 646 RELAD 650
Cdd:COG4372 348 VGLLD 352
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
411-665 |
4.45e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 411 QLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAALRVSE 490
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 491 GRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAglreppvppattdpfLLAESDEAKVQRAAagtgg 570
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA---------------ELQSEIAEREEELK----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 571 SLRAQVERLRQELQR---EQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHN-YVQMYRRNRQLEQELQQLSLELEAR 646
Cdd:COG4372 154 ELEEQLESLQEELAAleqELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKlIESLPRELAEELLEAKDSLEAKLGL 233
|
250
....*....|....*....
gi 261399904 647 ELADLGLSEPAPCICLEEI 665
Cdd:COG4372 234 ALSALLDALELEEDKEELL 252
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
403-472 |
4.77e-05 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 44.90 E-value: 4.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261399904 403 RQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 472
Cdd:pfam13851 95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
403-657 |
5.53e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 403 RQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQaelvqkgSELVALRVALREA 482
Cdd:pfam01576 492 RQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ-------RELEALTQQLEEK 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 483 RAALRVSEGRARGLQEaararelELEACSQELQRYRQEAEQLREKARHLDAeaaglreppvppattdpfLLAESDEAKVQ 562
Cdd:pfam01576 565 AAAYDKLEKTKNRLQQ-------ELDDLLVDLDHQRQLVSNLEKKQKKFDQ------------------MLAEEKAISAR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 563 RAAAGTggslRAQVERLRQE-----LQREQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQ 637
Cdd:pfam01576 620 YAEERD----RAEAEAREKEtralsLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE 695
|
250 260
....*....|....*....|.
gi 261399904 638 QLSLELEarELAD-LGLSEPA 657
Cdd:pfam01576 696 EMKTQLE--ELEDeLQATEDA 714
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
333-640 |
6.89e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 333 KLRDREAELQQLRDSVDESEAAVCQAFGARQRRWPGEREDCASHAQQAT------QRVQRAQQLLQLQVFQLQQEKRQLQ 406
Cdd:pfam07888 98 ELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLeretelERMKERAKKAGAQRKEEEAERKQLQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 407 ddfAQLLQEREQLERRCATFereqQELGPRLEETKWEVCQKSGEISLLKQQLKESQaelvQKGSELVALRVALREARAAL 486
Cdd:pfam07888 178 ---AKLQQTEEELRSLSKEF----QELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEALLEELRSLQERL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 487 RVSEGRARGLQEAARARELELEACSQELQRYRQEAEQ-----------LREKARHLDAEAAGLREPpvppattdpfllAE 555
Cdd:pfam07888 247 NASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQltlqladaslaLREGRARWAQERETLQQS------------AE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 556 SDEAKVQRAAA------GTGGSLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRN 629
Cdd:pfam07888 315 ADKDRIEKLSAelqrleERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYI 394
|
330
....*....|.
gi 261399904 630 RQLEQELQQLS 640
Cdd:pfam07888 395 RQLEQRLETVA 405
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
410-644 |
1.64e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 410 AQLLQEREQLE--RRCATFEREQQelgpRLEETKWEVCQKsgEISLLKQQLKESQAELVQKGSELVALRVALREARAALR 487
Cdd:TIGR00618 166 KELLMNLFPLDqyTQLALMEFAKK----KSLHGKAELLTL--RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 488 VSEGRARGLQEAARARELELEACSQ---ELQRYRQEAEQLREKARHLDAEAAGLREPPVPPATTDPFLLAESDEAKVQRA 564
Cdd:TIGR00618 240 QSHAYLTQKREAQEEQLKKQQLLKQlraRIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 565 AAGTGGSLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQ----LEQELQQLS 640
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQqkttLTQKLQSLC 399
|
....
gi 261399904 641 LELE 644
Cdd:TIGR00618 400 KELD 403
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
404-647 |
1.76e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 404 QLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKwEVCQKSGEisllkqQLKESQAELVQKGSELVALRVALREAR 483
Cdd:PRK04863 331 QAASDHLNLVQTALRQQEKIERYQADLEELEERLEEQN-EVVEEADE------QQEENEARAEAAEEEVDELKSQLADYQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 484 AALRVSEGRARGLQEAARARE----------LELEACSQELQRYRQEAEQLREKARHL-----DAEAAGLR--------- 539
Cdd:PRK04863 404 QALDVQQTRAIQYQQAVQALErakqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLeqklsVAQAAHSQfeqayqlvr 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 540 --EPPVPPATTDPFLLAESDEAKVQRAAAGTGGSLRAQ-------------VERLRQELQREQRRGDEQRNSFEGERLAW 604
Cdd:PRK04863 484 kiAGEVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRlseleqrlrqqqrAERLLAEFCKRLGKNLDDEDELEQLQEEL 563
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 261399904 605 QAEKEQVIRYQKQLQHNYVQMyrrnRQLEQELQQLSLELEARE 647
Cdd:PRK04863 564 EARLESLSESVSEARERRMAL----RQQLEQLQARIQRLAARA 602
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
334-651 |
1.97e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 334 LRDREAELQQLRDSVDESEAAVCQAFGARQRRWPGEREDCASHAQQATQRVQRAQQLLQLQVFQLQQEKRQLQD--DFAQ 411
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 412 LLQEREQLERRCATF-----------------------------------------EREQQELGPRLEETKWEVCQKSGE 450
Cdd:COG4717 238 AAALEERLKEARLLLliaaallallglggsllsliltiagvlflvlgllallflllAREKASLGKEAEELQALPALEELE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 451 ISLLKQQLKESQAELVQKGSELVALRVALREARAALRVSEGRARGLQEAARAREL-------------ELEACSQELQRY 517
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeagvedeeELRAALEQAEEY 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 518 RQEAEQLREKARHLDAEAAGLREppVPPATTDPFLLAESDEAKVQRAAagtggsLRAQVERLRQELQREQRRGDEQRNSf 597
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEE--LLEALDEEELEEELEELEEELEE------LEEELEELREELAELEAELEQLEED- 468
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 261399904 598 egERLawqAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQQLSLELEARELADL 651
Cdd:COG4717 469 --GEL---AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPV 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
407-639 |
2.32e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 407 DDFAQLLQEREQLERR---CATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREAR 483
Cdd:COG1196 554 EDDEVAAAAIEYLKAAkagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 484 AALRVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREppvppattdpFLLAESDEAKVQR 563
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE----------EELELEEALLAEE 703
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261399904 564 AAAGTGGSLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQQL 639
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
499-647 |
2.69e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 499 AARAReLELEACSQELQRYRQEAEQLR-EKARhldaeaaglreppvppattdpfLLAESDEAKVQRAAAgtggsLRAQVE 577
Cdd:COG0542 399 AARVR-MEIDSKPEELDELERRLEQLEiEKEA----------------------LKKEQDEASFERLAE-----LRDELA 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 578 RLRQELQREQRRgdeqrnsfegerlaWQAEKEQVIRYQKqLQHNYVQMYRRNRQLEQELQQLSLELEARE 647
Cdd:COG0542 451 ELEEELEALKAR--------------WEAEKELIEEIQE-LKEELEQRYGKIPELEKELAELEEELAELA 505
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
401-581 |
2.90e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAEL--VQKGSELVALRVA 478
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 479 LREARAALRVSEGRARGLQEAARARELELEACSQELQryrQEAEQLREKARHLDAEAAGLReppvppattdpfllAESDE 558
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELE--------------AELEE 160
|
170 180
....*....|....*....|....*
gi 261399904 559 AKVQRA--AAGTGGSLRAQVERLRQ 581
Cdd:COG1579 161 LEAEREelAAKIPPELLALYERIRK 185
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
454-529 |
4.43e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 41.03 E-value: 4.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261399904 454 LKQQLKESQAELVQKGSELVALRVALREARAALRvsegrarglQEAARARELELEACSQELQRYRQEAEQLREKAR 529
Cdd:smart00935 23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS---------EAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
405-647 |
4.51e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 405 LQDDFAQLLQEREQLERRCATFEREQQELGPRLEETkwEVCQKSGEISLLKQQLKESQ-----AELVQKGSELVALRVAL 479
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEA--EALLEAGKCPECGQPVEGSPhvetiEEDRERVEELEAELEDL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 480 REARAALRVSEGRARGLQEAARARELELEACS----------QELQRYRQEAEQLREKARHLDAEAAGLREppvppATTD 549
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREdleeliaerrETIEEKRERAEELRERAAELEAEAEEKRE-----AAAE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 550 PFLLAES------------DEAKVQRAAAGTGGSLRAQVERLRQELQ--REQRRGDEQRNSFEGERLAwqAEKEQVIRYQ 615
Cdd:PRK02224 563 AEEEAEEareevaelnsklAELKERIESLERIRTLLAAIADAEDEIErlREKREALAELNDERRERLA--EKRERKRELE 640
|
250 260 270
....*....|....*....|....*....|...
gi 261399904 616 KQLQHNYVQMYRRNRQ-LEQELQQLSLELEARE 647
Cdd:PRK02224 641 AEFDEARIEEAREDKErAEEYLEQVEEKLDELR 673
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
402-535 |
4.60e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 402 KRQLQDDFAQLLQEREQLERRCATFEREQQElgprLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVAlrE 481
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEE----LEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE--E 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 261399904 482 ARAAL--RVsEGRARgLQEAARARELELEAcsqelqryRQEAEQlreKARHLDAEA 535
Cdd:PRK12704 155 AKEILleKV-EEEAR-HEAAVLIKEIEEEA--------KEEADK---KAKEILAQA 197
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
454-529 |
5.52e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 41.36 E-value: 5.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261399904 454 LKQQLKESQAELVQKGSELVALRVALREARAALRvsegrarglQEAARARELELEACSQELQRYRQEAEQLREKAR 529
Cdd:COG2825 48 LEKEFKKRQAELQKLEKELQALQEKLQKEAATLS---------EEERQKKERELQKKQQELQRKQQEAQQDLQKRQ 114
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
437-644 |
6.38e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 437 LEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAALRvsegrarglQEAARARElELEACSQELQR 516
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELR---------EEAQELRE-KRDELNEKVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 517 YRQEAEQLREKARHLDAEAAGLREppvppattdpfllaesdEAKVQRAAAGTGGSLRAQVERLRQELQREQRRGDEQRNS 596
Cdd:COG1340 76 LKEERDELNEKLNELREELDELRK-----------------ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKEL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 261399904 597 FEG-ERLAWQAEK-EQVIRYQKQLqhnyvqmyrrnRQLEQELQQLSLELE 644
Cdd:COG1340 139 VEKiKELEKELEKaKKALEKNEKL-----------KELRAELKELRKEAE 177
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
326-648 |
6.82e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 326 LHCVLEGKLRDREAELQQlRDSVDESEAAVCQAFGARQRRWPGEREDCASHAQQATQRVQRAQQLLQLQVFqlqqekRQL 405
Cdd:TIGR00618 312 IHTELQSKMRSRAKLLMK-RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI------HTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 406 QDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKS---GEISLLKQQLKESQAELVQKGSELVALRVALREA 482
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAhakKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 483 RAALRVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREPPV--PP--------------- 545
Cdd:TIGR00618 465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPltRRmqrgeqtyaqletse 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 546 ATTDPFLLAE-----SDEAKVQRAAAGTGG------SLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEqviry 614
Cdd:TIGR00618 545 EDVYHQLTSErkqraSLKEQMQEIQQSFSIltqcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR----- 619
|
330 340 350
....*....|....*....|....*....|....
gi 261399904 615 QKQLQHNYVQMYRRNRQLEQELQQLSLELEAREL 648
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQL 653
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
322-541 |
7.45e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 322 DEALLHcvLEGKLRDREAELQQ----------LRDSVDESEAAvcQAFGARQRRWPGERedcaSHAQQATQRvqRAQQLL 391
Cdd:PRK04863 455 TEELLS--LEQKLSVAQAAHSQfeqayqlvrkIAGEVSRSEAW--DVARELLRRLREQR----HLAEQLQQL--RMRLSE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 392 QLQVFQLQQEKRQLQDDFAQLLQEREQLErrcATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELvqkgSE 471
Cdd:PRK04863 525 LEQRLRQQQRAERLLAEFCKRLGKNLDDE---DELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARI----QR 597
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261399904 472 LVALRVALREARAALrvsegrARgLQEAARARELELEACSQELQR-------YRQEAEQLREKARHLDAEAAGLREP 541
Cdd:PRK04863 598 LAARAPAWLAAQDAL------AR-LREQSGEEFEDSQDVTEYMQQllerereLTVERDELAARKQALDEEIERLSQP 667
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
466-643 |
1.45e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 466 VQKGSELVALRVALREARAALRVSEGRARGLQEaararelELEACSQELQRYRQEAEQLREKARHLDAEAAGLREppvpp 545
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEK-------ALAELRKELEELEEELEQLRKELEELSRQISALRK----- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 546 attdpflLAESDEAKVQRAAAgtggsLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQM 625
Cdd:TIGR02168 734 -------DLARLEAEVEQLEE-----RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
170
....*....|....*...
gi 261399904 626 YRRNRQLEQELQQLSLEL 643
Cdd:TIGR02168 802 REALDELRAELTLLNEEA 819
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
330-586 |
1.47e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 330 LEGKLRDREAELQQLRDSVDESEAAVC----QAFGARQRRWPGEREDCA--SHAQQATQRVQRAQQLLQLQVFQLQ---Q 400
Cdd:pfam19220 95 LEAALREAEAAKEELRIELRDKTAQAEalerQLAAETEQNRALEEENKAlrEEAQAAEKALQRAEGELATARERLAlleQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKW------------------EVCQKSGEISLLKQQLKESQ 462
Cdd:pfam19220 175 ENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGqlaaeqaereraeaqleeAVEAHRAERASLRMKLEALT 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 463 AELVQKGSELVALRVALREARAALRVSEGRARGLQEAARARELELEACSQELQRYR---QEAEQLR----EKARHLdAEA 535
Cdd:pfam19220 255 ARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTqqfQEMQRARaeleERAEML-TKA 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 261399904 536 AGLREPPVPPATTDPFLLAESDEAKVQRAAAgTGGSLRAQVERLRQELQRE 586
Cdd:pfam19220 334 LAAKDAALERAEERIASLSDRIAELTKRFEV-ERAALEQANRRLKEELQRE 383
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
498-639 |
1.80e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 498 EAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREppvppattdpfllaesdeakvQRAAagtggsLRAQVE 577
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAE---------------------KRDE------LNAQVK 53
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261399904 578 RLRQELQ--REQRRGD-EQRNSFEGERLAWQAEKEQV---IRYQKQLQHNYVQMYRRNRQLEQELQQL 639
Cdd:COG1340 54 ELREEAQelREKRDELnEKVKELKEERDELNEKLNELreeLDELRKELAELNKAGGSIDKLRKEIERL 121
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
325-646 |
1.98e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 325 LLHCVLEGKLRDReAELQQLRDSVDESEAAVCQAFGARQRRWPGEREDCASHAQQATQRVQRAQQLLQLQVFQLQQEKR- 403
Cdd:pfam07888 31 LLQNRLEECLQER-AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAs 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 404 --QLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKE-------SQAELVQKGSELVA 474
Cdd:pfam07888 110 seELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEeeaerkqLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 475 LRVALREARAALRVSEGRARGLQE----------AARARELELEACSQELQryrqeaeQLREKARHLDAEAAGLREPPVP 544
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDtittltqkltTAHRKEAENEALLEELR-------SLQERLNASERKVEGLGEELSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 545 PATTDPFLLAESDEAKVQRAA-----AGTGGSLRA---------------------QVERLRQELQREQRRGDEQRNSFE 598
Cdd:pfam07888 263 MAAQRDRTQAELHQARLQAAQltlqlADASLALREgrarwaqeretlqqsaeadkdRIEKLSAELQRLEERLQEERMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 261399904 599 GERLAWQAEKE----QVIRYQKQLQH-----NYVQMYRRNRQLE-QELQQLSLELEAR 646
Cdd:pfam07888 343 KLEVELGREKDcnrvQLSESRRELQElkaslRVAQKEKEQLQAEkQELLEYIRQLEQR 400
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
382-650 |
2.28e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 382 QRVQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQ--EREQLERRCATFEREQQELGPRL-----EETKWEVCQKSGEISLL 454
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 455 KQQLKESQAELVQKGSELVALRVALREARAALRVSEGRARGLQEAARARELELEACSQELQRYRQE---AEQLREKARHL 531
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakkAEELKKKEAEE 1714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 532 DAEAAGLREppvppattdpfllaESDEAKVQraaagtggslraqVERLRQELQREQRRGDEQRNSfEGERLAWQAEKEQV 611
Cdd:PTZ00121 1715 KKKAEELKK--------------AEEENKIK-------------AEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEE 1766
|
250 260 270
....*....|....*....|....*....|....*....
gi 261399904 612 IRYQKQLQHNYVQMYRRNRQLEQELQQLSLELEARELAD 650
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
454-529 |
2.60e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 38.71 E-value: 2.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261399904 454 LKQQLKESQAELVQKGSELVALRVALREARAALrvsegrarglQEAARARELELEACSQELQRYRQEAEQLREKAR 529
Cdd:pfam03938 24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALL----------EEEREEKEQELQKKEQELQQLQQKAQQELQKKQ 89
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
454-647 |
3.21e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 454 LKQQLKESQAELVQkgselvaLRVALREARAALRVSEGRARGLQEAARARELEleacsQELQRYRQEAEQLREKARHLdA 533
Cdd:COG3206 180 LEEQLPELRKELEE-------AEAALEEFRQKNGLVDLSEEAKLLLQQLSELE-----SQLAEARAELAEAEARLAAL-R 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 534 EAAGLREPPVPPATTDPF---LLAESDEAKVQRAAAGTG-GSLRAQVERLRQELQR-EQRRGDEQRNSFEGERLAWQAEK 608
Cdd:COG3206 247 AQLGSGPDALPELLQSPViqqLRAQLAELEAELAELSARyTPNHPDVIALRAQIAAlRAQLQQEAQRILASLEAELEALQ 326
|
170 180 190
....*....|....*....|....*....|....*....
gi 261399904 609 EQVIRYQKQLQhNYVQMYRRNRQLEQELQQLSLELEARE 647
Cdd:COG3206 327 AREASLQAQLA-QLEARLAELPELEAELRRLEREVEVAR 364
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
338-545 |
3.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 338 EAELQQLRDSVDESEAAVcQAFgaRQRRW----PGEREDCASHAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDD----- 408
Cdd:COG3206 181 EEQLPELRKELEEAEAAL-EEF--RQKNGlvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 409 -------FAQLLQEREQLERRCATFEREQQELGPRLEETKwevcqksGEISLLKQQLKESQAELVQkgsELVALRVALRE 481
Cdd:COG3206 258 ellqspvIQQLRAQLAELEAELAELSARYTPNHPDVIALR-------AQIAALRAQLQQEAQRILA---SLEAELEALQA 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 482 ARAALRVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAG------LREPPVPP 545
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALtvgnvrVIDPAVVP 397
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
330-541 |
3.45e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 330 LEGKLRDREAELQQLrdsvDESEAAVCQAFGA--RQRRWPGERE---DCASHAQQATQRVQ-RAQQLLQLQVFQLQQEKR 403
Cdd:COG3096 460 LEQKLSVADAARRQF----EKAYELVCKIAGEveRSQAWQTAREllrRYRSQQALAQRLQQlRAQLAELEQRLRQQQNAE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 404 QLQDDFAQllQEREQLERRcATFEREQQELGPRLEEtkwevcqksgeisllkqqLKESQAELVQKGSELVALRVALREAR 483
Cdd:COG3096 536 RLLEEFCQ--RIGQQLDAA-EELEELLAELEAQLEE------------------LEEQAAEAVEQRSELRQQLEQLRARI 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261399904 484 AALRVSEGRARGLQEAA-RARELELE--ACSQELQRYRQ-----------EAEQLREKARHLDAEAAGLREP 541
Cdd:COG3096 595 KELAARAPAWLAAQDALeRLREQSGEalADSQEVTAAMQqllerereatvERDELAARKQALESQIERLSQP 666
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
401-539 |
3.85e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.24 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDfAQLLQEREQLERRCATFERE----QQELgpRLE-ETKWEVCQKSGEI-SLLKQQLKESQAELVQKGSElva 474
Cdd:COG2268 218 QANREAEE-AELEQEREIETARIAEAEAElakkKAEE--RREaETARAEAEAAYEIaEANAEREVQRQLEIAERERE--- 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261399904 475 lrVALREARAALRVSEGRA-RGLQEAARARELELEAcsqelqryRQEAEQLREKARhldAEAAGLR 539
Cdd:COG2268 292 --IELQEKEAEREEAELEAdVRKPAEAEKQAAEAEA--------EAEAEAIRAKGL---AEAEGKR 344
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
329-583 |
4.10e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 329 VLEGKLRDREAELQQLRDSVdeseAAVcqafGARQRRWPGEREDCASHAQQATQRVQRAqqllqlqvfqlqqekrqlqdd 408
Cdd:COG1842 27 MLDQAIRDMEEDLVEARQAL----AQV----IANQKRLERQLEELEAEAEKWEEKARLA--------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 409 faqLLQEREQLERRCATferEQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAALRV 488
Cdd:COG1842 78 ---LEKGREDLAREALE---RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 489 SEgRARGLQEAARARELEleacsqelqryrqeaeQLREKARHLDAEAAGLREppvppattdpflLAESDEAKVQRAAAGT 568
Cdd:COG1842 152 NE-ALSGIDSDDATSALE----------------RMEEKIEEMEARAEAAAE------------LAAGDSLDDELAELEA 202
|
250
....*....|....*
gi 261399904 569 GGSLRAQVERLRQEL 583
Cdd:COG1842 203 DSEVEDELAALKAKM 217
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
401-662 |
4.15e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 401 EKRQLQDDFAQLLQERE------QLERRCATFEREQQELG---PRLEET--------KW-----------EVCQKSGEIS 452
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREaqeeqlKKQQLLKQLRARIEELRaqeAVLEETqerinrarKAaplaahikavtQIEQQAQRIH 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 453 LLKQQLKESQAELVQKGSELVALRVALREARAALRV---SEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKAR 529
Cdd:TIGR00618 314 TELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQ 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 530 HLDAEAAGLREPPVPPATTDPFLLAESDEaKVQRAAAgtGGSLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKE 609
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDL-QGQLAHA--KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261399904 610 QVirYQKQLQHNYVQMYRRNRQLE----QELQQLSLELEAR------ELADLGLSEPAPCICL 662
Cdd:TIGR00618 471 RE--QQLQTKEQIHLQETRKKAVVlarlLELQEEPCPLCGScihpnpARQDIDNPGPLTRRMQ 531
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
404-610 |
4.93e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.52 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 404 QLQDDFAQLLQEREQLE-RRCATFEREQQElgpRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVAL--- 479
Cdd:pfam13868 137 EEQAEWKELEKEEEREEdERILEYLKEKAE---REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyqe 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 480 ----REARAALRVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKArhLDAEAAGLReppvppattdpfLLAE 555
Cdd:pfam13868 214 eqerKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM--LRKQAEDEE------------IEQE 279
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 261399904 556 SDEAKVQRAAAgtggsLRAQVERLRQElQREQRRGDEQRNSFEGERLAWQAEKEQ 610
Cdd:pfam13868 280 EAEKRRMKRLE-----HRRELEKQIEE-REEQRAAEREEELEEGERLREEEAERR 328
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
336-625 |
4.96e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 336 DREAELQQLRDSVDESEAAVcqafgarqrrwpgerEDCASHAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQE 415
Cdd:PRK04863 834 DPEAELRQLNRRRVELERAL---------------ADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEE 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 416 -REQLERrCATFEREQQELGPRLEETKWEVC---QKSGEISLLKQQLKESQAEL--VQKG----SELVALRVALREARAA 485
Cdd:PRK04863 899 iREQLDE-AEEAKRFVQQHGNALAQLEPIVSvlqSDPEQFEQLKQDYQQAQQTQrdAKQQafalTEVVQRRAHFSYEDAA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 486 LRVSEGRArgLQEAARAReleLEACSQELQRYRQEAEQLREKARHLDAEAAGLREPPVPPATTDPFLLAESDEAKVqRAA 565
Cdd:PRK04863 978 EMLAKNSD--LNEKLRQR---LEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGV-PAD 1051
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 566 AGTGGSLRAQVERLRQELqreqRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQM 625
Cdd:PRK04863 1052 SGAEERARARRDELHARL----SANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
413-650 |
5.19e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 413 LQEREQLERRCATFEreqqELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVAL----------REA 482
Cdd:COG3096 343 LRQQEKIERYQEDLE----ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvqqtraiqyQQA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 483 RAALRvsegRARGLQEAArarELELEACSQELQRYRQEAEQLREKARHL-----DAEAAGLREPPVppattdpFLLAESD 557
Cdd:COG3096 419 VQALE----KARALCGLP---DLTPENAEDYLAAFRAKEQQATEEVLELeqklsVADAARRQFEKA-------YELVCKI 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 558 EAKVQRAAAG--------TGGSLRAQVER---LRQELQREQRRGDEQRNSfegERLAwqaeKEQVIRYQKQLQHNY-VQM 625
Cdd:COG3096 485 AGEVERSQAWqtarellrRYRSQQALAQRlqqLRAQLAELEQRLRQQQNA---ERLL----EEFCQRIGQQLDAAEeLEE 557
|
250 260
....*....|....*....|....*
gi 261399904 626 YrrnrQLEQELQQLSLELEARELAD 650
Cdd:COG3096 558 L----LAELEAQLEELEEQAAEAVE 578
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
406-645 |
5.99e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 406 QDDFAQLLQE-REQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQ-------------LKESQAELVQKGSE 471
Cdd:pfam12128 414 EDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenfderierareeQEAANAEVERLQSE 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 472 LVALRVALREARAALRVSEGRARGLQEAARARELELEACSQELQRY-RQEAEQLREKARHLDAEAAGLREPPVPPATTD- 549
Cdd:pfam12128 494 LRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFlRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGs 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 550 -------------------PFLLAESDEAKVQRAAA----GTGGSLRAQVER----LRQELQREQRRGDEQRNSFEGERL 602
Cdd:pfam12128 574 vggelnlygvkldlkridvPEWAASEEELRERLDKAeealQSAREKQAAAEEqlvqANGELEKASREETFARTALKNARL 653
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 261399904 603 A---WQAEKEQV-IRYQKQLQHNYVQMYRRNRQLEQELQQLSLELEA 645
Cdd:pfam12128 654 DlrrLFDEKQSEkDKKNKALAERKDSANERLNSLEAQLKQLDKKHQA 700
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
552-643 |
6.02e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.56 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 552 LLAESDEAKVQRAAagtggsLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQViryQKQLQHNYVQMYRRNRQ 631
Cdd:pfam03938 10 ILEESPEGKAAQAQ------LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEK---EQELQKKEQELQQLQQK 80
|
90
....*....|..
gi 261399904 632 LEQELQQLSLEL 643
Cdd:pfam03938 81 AQQELQKKQQEL 92
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
410-534 |
6.42e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 38.86 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 410 AQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAALRVS 489
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261399904 490 EGRARGLQEAARARELELEAC---------------------SQELQRYRQEAEQLREKARHLDAE 534
Cdd:pfam00261 84 ENRALKDEEKMEILEAQLKEAkeiaeeadrkyeevarklvvvEGDLERAEERAELAESKIVELEEE 149
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
378-566 |
6.68e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.40 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 378 QQATQRVQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQEREQlERRCATFEREQQELGPRLEETKwevcQKSGEisllKQQ 457
Cdd:PRK09510 68 QQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK-ERLAAQEQKKQAEEAAKQAALK----QKQAE----EAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 458 LKESQAELVQKGSELVALRVALREARA-ALRVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAA 536
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAAKKAAAeAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKK 218
|
170 180 190
....*....|....*....|....*....|
gi 261399904 537 GLREPPVPPATTdpfllAESDEAKVQRAAA 566
Cdd:PRK09510 219 AAAEAKAAAAKA-----AAEAKAAAEKAAA 243
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
330-640 |
7.35e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.55 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 330 LEGKLRDREAELQQLRDSVDESE---AAVCQAFGARQRRwpgeredcASHAQQATQRVQRAQQLLQLQV-FQLQQEKRQ- 404
Cdd:COG3096 373 AAEQLAEAEARLEAAEEEVDSLKsqlADYQQALDVQQTR--------AIQYQQAVQALEKARALCGLPDlTPENAEDYLa 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 405 -LQDDFAQLLQEREQLERRCATFE--REQQELGPRLeetkweVCQKSGEISllKQQLKESQAELVQKGSELVALrvALRE 481
Cdd:COG3096 445 aFRAKEQQATEEVLELEQKLSVADaaRRQFEKAYEL------VCKIAGEVE--RSQAWQTARELLRRYRSQQAL--AQRL 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 482 ARAALRVSEGRARgLQEAARARELeLEACSQELQRYRQEAEQLREKARHLDAEAAGLREppvppattdpfLLAESDEAKV 561
Cdd:COG3096 515 QQLRAQLAELEQR-LRQQQNAERL-LEEFCQRIGQQLDAAEELEELLAELEAQLEELEE-----------QAAEAVEQRS 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261399904 562 QraaagtggsLRAQVERLRQELQREQRRGDEQRNSFEG-ERLAWQ------------AEKEQVIRYQKQLQHNYVQMYRR 628
Cdd:COG3096 582 E---------LRQQLEQLRARIKELAARAPAWLAAQDAlERLREQsgealadsqevtAAMQQLLEREREATVERDELAAR 652
|
330
....*....|..
gi 261399904 629 NRQLEQELQQLS 640
Cdd:COG3096 653 KQALESQIERLS 664
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
459-535 |
7.87e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.55 E-value: 7.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261399904 459 KESQAELVQKGSELVALRVALREARAALRVSEGRARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEA 535
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQER 214
|
|
| |
